Ligand peroxynitrite

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Basic Ligand Information

Molecular Structure
Picture of peroxynitrite (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
HNO3
peroxynitrite
PUZFEBZBSNCBNS-YRVFCXMDSA-N
Synonyms:
ONOO-, peroxinitrite

Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (10 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
peroxynitrite + 4-hydroxyphenylacetic acid + NADPH + H+ = 4-hydroxyl-3-nitro-phenylacetic acid + NADP+ + H2O
show the reaction diagram
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peroxynitrite + NADPH = nitrite + H2O + NADP+
show the reaction diagram
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peroxynitrite = NO + O22-
show the reaction diagram
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Product in Enzyme-catalyzed Reactions (2 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE

Activator in Enzyme-catalyzed Reactions (4 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
peroxynitrite activates by oxidizing cysteine resiudes to sulfenic acid. C298 is the major site of sulfenic acid formation and oxidation of C298 is necessary and sufficient for enzyme activation by peroxynitrite
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peroxidase activity, MS-analysis reveals that tyrosine 385 is a target for nitration by ONOO- only when heme is present
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peroxynitrite specifically activates the acidic sphingomyelinase
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activation in presence of GSH
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Inhibitor in Enzyme-catalyzed Reactions (46 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
0.1 mM, 50% inhibition of cysteine-free mutant C85S/C152E, no inhibition of wild-type
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exclusively nitrates residues Tyr213, Try292, and Tyr345. Tyr345 is found at 3.3 A of His313, which is involved in the NADP-binding site. Nitration of residue Tyr345 is responsible for inhibition
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nitrating conditions after exposure to peroxynitrite strongly inhibit enzyme activity. Among the isoforms, cytosolic OASA1 is markedly sensitive to nitration. Nitration assays on purified recombinant OASA1 protein lead to 90% reduction of the activity due to inhibition of the enzyme. Inhibition of OASA1 activity upon nitration correlates with the identification of a modified OASA1 protein containing a 3-nitroTyr302 residue. Inhibition caused by Tyr302 nitration on OASA1 activity seems to be due to a drastically reduced O-acetylserine substrate binding to the nitrated protein, and also to reduced stabilization of the pyridoxal-5-phosphate cofactor through hydrogen bonds
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irreversible inhibition of nSMase1
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causes nitration on several tyrosine residues including Tyr383 and Tyr466
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in isolated nonsynaptic brain mitochondria Lon protease is highly susceptible to oxidative inactivation by peroxynitrite. This susceptibility is more pronounced with regard to ATP-stimulated activity, which is inhibited by 75% in the presence of a bolus addition of 1 mM ONOO, whereas basal unstimulated activity is inhibited by 45%. A decline in Lon protease activity precedes electron transport chain dysfunction and ATP-stimulated activity is approximately fivefold more sensitive than basal Lon protease activity. Supplementation of mitochondrial matrix extracts with reduced glutathione, following peroxynitrite exposure, results in partial restoration of basal and ATP-stimulated activity
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50% inhibition at 280 microM and an enzyme concentration of 10 microM
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0.01 mM, 50% inhibition
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formation of methionine sulfoxide by peroxynitrite at position 1606 of von Willebrand factor inhibits its cleavage by ADAMTS-13 a prothrombotic mechanism in diseases associated with oxidative stress, overview. Oxidation by peroxynitrite of purified VWF multimers inhibits ADAMTS-13 hydrolysis, but does not alter their electrophoretic pattern nor their ability to induce platelet agglutination by ristocetin. In vitro treatment of ADAMTS-13 with peroxynitrite over a concentration ranging from 0.050 to 0.250 mM causes a complete inhibition of the protease activity of the enzyme
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activity of wild-type enzyme is reduced to 38% in presence of peroxynitrite. Activities of mutants Y153A and Y253A are 233 completely abolished in the presence of peroxynitrite. Mutant Y146A shows 32% reduction in activity
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0.1 mM, 50% inhibition, almost complete inhibition above 1 mM, nitration of tyrosine residues
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decrease of Vmax and KM for fructose-1,6-bisphosphate after incubation with peroxynitrite. Tyrosine residues in the carboxyl-terminal region of the aldolase are major targets of nitration. Tyrosine nitration of aldolase A can contribute to an impaired cellular glycolytic activity
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exposure to peroxynitrite does not modify bound pyridoxal 5'-phosphate but leads to nitration of Trp208, Trp43 and Tyr223 and alterations in the heme environment including loss of thiolate coordination, conversion to high-spin and bleaching, with no detectable formation of oxoferryl compounds nor promotion of one-electron processes
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CPS1 activity is decreased by treatment with peroxynitrite in a peroxynitrite concentration- and time-dependent manner due to tyrosine nitration (47% decrease in 1 min and 60% decrease in 10 min with 1 mM peroxynitrite)
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addition of ONOO- to cytochrome bd in turnover with ascorbate and N,N,N',N'-tetramethyl-p-phenylenediamine causes the irreversible inhibition of about 15% of the enzyme fraction, due to the NO radical generated from ONOO-. Addition of ONOO- to cells expressing cytochrome bd as the only terminal oxidase, causes about 5% irreversible inhibition of O2 consumption. Purified cytochrome bd in turnover with O2 is able to metabolize ONOO- with an apparent turnover rate as high as about 10 mol ONOO- per mol of enzyme and per s at 25°C
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0.1 mM, complete inhibition
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Enzyme Kinetic Parameters

IC50 Value (7 results)

EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
0.15
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References & Links

Links to other databases for peroxynitrite

ChEBI
PubChem
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PubChem